1rc2
From Proteopedia
(New page: 200px<br /><applet load="1rc2" size="450" color="white" frame="true" align="right" spinBox="true" caption="1rc2, resolution 2.5Å" /> '''2.5 Angstrom Resoluti...) |
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| - | [[Image:1rc2.gif|left|200px]]<br /><applet load="1rc2" size=" | + | [[Image:1rc2.gif|left|200px]]<br /><applet load="1rc2" size="350" color="white" frame="true" align="right" spinBox="true" |
caption="1rc2, resolution 2.5Å" /> | caption="1rc2, resolution 2.5Å" /> | ||
'''2.5 Angstrom Resolution X-ray Structure of Aquaporin Z'''<br /> | '''2.5 Angstrom Resolution X-ray Structure of Aquaporin Z'''<br /> | ||
==Overview== | ==Overview== | ||
| - | Aquaporins are a family of water and small molecule channels found in | + | Aquaporins are a family of water and small molecule channels found in organisms ranging from bacteria to animals. One of these channels, the E. coli protein aquaporin Z (AqpZ), has been shown to selectively conduct only water at high rates. We have expressed, purified, crystallized, and solved the X-ray structure of AqpZ. The 2.5 A resolution structure of AqpZ suggests aquaporin selectivity results both from a steric mechanism due to pore size and from specific amino acid substitutions that regulate the preference for a hydrophobic or hydrophilic substrate. This structure provides direct evidence on the molecular mechanisms of specificity between water and glycerol in this family of channels from a single species. It is to our knowledge the first atomic resolution structure of a recombinant aquaporin and so provides a platform for combined genetic, mutational, functional, and structural determinations of the mechanisms of aquaporins and, more generally, the assembly of multimeric membrane proteins. |
==About this Structure== | ==About this Structure== | ||
| - | 1RC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with BGL as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http:// | + | 1RC2 is a [http://en.wikipedia.org/wiki/Single_protein Single protein] structure of sequence from [http://en.wikipedia.org/wiki/Escherichia_coli Escherichia coli] with <scene name='pdbligand=BGL:'>BGL</scene> as [http://en.wikipedia.org/wiki/ligand ligand]. Full crystallographic information is available from [http://oca.weizmann.ac.il/oca-bin/ocashort?id=1RC2 OCA]. |
==Reference== | ==Reference== | ||
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[[Category: Escherichia coli]] | [[Category: Escherichia coli]] | ||
[[Category: Single protein]] | [[Category: Single protein]] | ||
| - | [[Category: Egea, P | + | [[Category: Egea, P F.]] |
| - | [[Category: III, J | + | [[Category: III, J D.O Connell.]] |
| - | [[Category: Robles, Y | + | [[Category: Robles, Y C.]] |
| - | [[Category: Savage, D | + | [[Category: Savage, D F.]] |
| - | [[Category: Stroud, R | + | [[Category: Stroud, R M.]] |
[[Category: BGL]] | [[Category: BGL]] | ||
[[Category: aquaporin]] | [[Category: aquaporin]] | ||
[[Category: membrane protein]] | [[Category: membrane protein]] | ||
| - | ''Page seeded by [http:// | + | ''Page seeded by [http://oca.weizmann.ac.il/oca OCA ] on Thu Feb 21 14:49:16 2008'' |
Revision as of 12:49, 21 February 2008
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2.5 Angstrom Resolution X-ray Structure of Aquaporin Z
Overview
Aquaporins are a family of water and small molecule channels found in organisms ranging from bacteria to animals. One of these channels, the E. coli protein aquaporin Z (AqpZ), has been shown to selectively conduct only water at high rates. We have expressed, purified, crystallized, and solved the X-ray structure of AqpZ. The 2.5 A resolution structure of AqpZ suggests aquaporin selectivity results both from a steric mechanism due to pore size and from specific amino acid substitutions that regulate the preference for a hydrophobic or hydrophilic substrate. This structure provides direct evidence on the molecular mechanisms of specificity between water and glycerol in this family of channels from a single species. It is to our knowledge the first atomic resolution structure of a recombinant aquaporin and so provides a platform for combined genetic, mutational, functional, and structural determinations of the mechanisms of aquaporins and, more generally, the assembly of multimeric membrane proteins.
About this Structure
1RC2 is a Single protein structure of sequence from Escherichia coli with as ligand. Full crystallographic information is available from OCA.
Reference
Architecture and selectivity in aquaporins: 2.5 a X-ray structure of aquaporin Z., Savage DF, Egea PF, Robles-Colmenares Y, O'Connell JD 3rd, Stroud RM, PLoS Biol. 2003 Dec;1(3):E72. Epub 2003 Dec 22. PMID:14691544
Page seeded by OCA on Thu Feb 21 14:49:16 2008
